ArticleScientific reports2025
Effect of pH and buffer on substrate binding and catalysis by cis-aconitate decarboxylase.
Article in Scientific reports, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Robust structural, kinetic and biophysical characterization of wild-type human ACOD1, selected mutants and their interaction with citraconate.Journal of structural biology: X · 2026Article
- Offense and defense: itaconate mediates bidirectional immune regulation of host-bacteria interaction.Journal of biomedical science · 2026Review
- Ionic Liquid-Mediated Modulation of Zwitterionic Micelles and Their Catalytic Performance in the Decarboxylation of 6‑NBIC.ACS omega · 2026Article
- Morphable 'Stitched' Sensors for Simultaneous Spatiotemporal Tracking of Correlated Bioanalytes in Living Cells.JACS Au · 2026Article
- Identification of novel metagenomic lipases through integrated structural and sequence-based analysis.PeerJ · 2026Article
- Mn Oxide Nanowire/ZIF-8 Composites with Multiple Enzyme-like Activities for Enantioselective Glutamate Sensing.Biosensors · 2025Article
- Spectroscopic method for measuring activity of cis-aconitate decarboxylase, an important metabolic regulator of immune responses.Analytical biochemistry · 2025Article
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
cis-Aconitate decarboxylase (ACOD1, CAD, IRG1) catalyses the synthesis of itaconic acid in activated myeloid cells such as macrophages. Several histidine residues in the active site bind the substrate and enable the decarboxylation reaction. The in vitro activity of ACOD1 enzymes is commonly determined by incubation with substrate, followed by HPLC measurement of itaconic acid production. Phosphate buffers have often been used for this assay. However, the influence of buffer type on enzyme activity has not been investigated. Here, the effect of buffer and pH on enzyme kinetics of human and mouse ACOD1 and Aspergillus terreus CAD was investigated. It was found that high concentrations of phosphate inhibit the three enzymes. An alternative buffer was selected and the assay was adapted to the 96-well microtitre plate format for increased throughput. Enzyme kinetics were determined in the pH range of 5.5-8.25. A strong increase of K
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